ID Q0CCY8_ASPTN Unreviewed; 343 AA.
AC Q0CCY8;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=enoyl-[acyl-carrier-protein] reductase {ECO:0000256|ARBA:ARBA00038963};
DE EC=1.3.1.104 {ECO:0000256|ARBA:ARBA00038963};
GN ORFNames=ATEG_08446 {ECO:0000313|EMBL:EAU31619.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU31619.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.104;
CC Evidence={ECO:0000256|ARBA:ARBA00035831};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC {ECO:0000256|ARBA:ARBA00010371}.
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DR EMBL; CH476605; EAU31619.1; -; Genomic_DNA.
DR RefSeq; XP_001217067.1; XM_001217067.1.
DR AlphaFoldDB; Q0CCY8; -.
DR STRING; 341663.Q0CCY8; -.
DR EnsemblFungi; EAU31619; EAU31619; ATEG_08446.
DR GeneID; 4353096; -.
DR VEuPathDB; FungiDB:ATEG_08446; -.
DR eggNOG; KOG0025; Eukaryota.
DR HOGENOM; CLU_026673_17_0_1; -.
DR OMA; LIYETAN; -.
DR OrthoDB; 6213at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd08290; ETR; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43981; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43981:SF2; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, MITOCHONDRIAL; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007963};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 8..328
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 343 AA; 36944 MW; 7E8E5EACDAF739B6 CRC64;
MAQSLVHSSS DGSHLVNHPI PSITGPDQVL VQMSAAPVNR VDLMTLANLY PVKPHYRVDG
DPIPGFDGCG VVLASSSPSF DPGDLVLPRI LGLGTWRTHA VWPASSLLKL PNNTPPVAGA
LLRSGALVAW LLCEHVTPLS SGEWVLLSAG TSCVSQFFVQ FARLKGINTI LVIRDRDNIE
ITRERLLALG ASLVVTESEL SQATESSHPG RAVLALDSVF GRVGEDLARL LSPGGKFVMV
GMLAGPKTSI NVSAEHLFQK QLSFLPFRSS EVLKRMGDEQ AMEVIQHVAT LLADGRVVMP
ELNCVRWESS MSDGETKKAL EAAQSREVGY KKTVWVFAPR PSV
//
